about
Structure, mechanism and cooperation of bacterial multidrug transportersStructure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded stateMolecular properties of bacterial multidrug transportersTuning the drug efflux activity of an ABC transporter in vivo by in vitro selected DARPin bindersHoechst 33342 Is a Hidden "Janus" amongst Substrates for the Multidrug Efflux Pump LmrPBasic residues R260 and K357 affect the conformational dynamics of the major facilitator superfamily multidrug transporter LmrPThe homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanismRelocation of active site carboxylates in major facilitator superfamily multidrug transporter LmrP reveals plasticity in proton interactionsATP-dependent substrate transport by the ABC transporter MsbA is proton-coupledPlasmodium falciparum expresses a multidrug resistance-associated proteinThe secondary multidrug transporter LmrP contains multiple drug interaction sites.The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids.Recent developments in the biochemistry and ecology of enhanced biological phosphorus removal.The lactococcal secondary multidrug transporter LmrP confers resistance to lincosamides, macrolides, streptogramins and tetracyclines.The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities.Drug-lipid A interactions on the Escherichia coli ABC transporter MsbA.Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus.Functional role of transmembrane helix 6 in drug binding and transport by the ABC transporter MsbA.A multidrug ABC transporter with a taste for salt.Multidrug transport protein norM from vibrio cholerae simultaneously couples to sodium- and proton-motive force.β-Lactam selectivity of multidrug transporters AcrB and AcrD resides in the proximal binding pocket.Multidrug resistance in lactic acid bacteria: molecular mechanisms and clinical relevance.Structure and function of multidrug transporters.Structure-function analysis of multidrug transporters in Lactococcus lactis.Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.Molecular pharmacological characterization of two multidrug transporters in Lactococcus lactis.Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis.Membrane-bound ATPase contributes to hop resistance of Lactobacillus brevis.Molecular basis of multidrug transport by ATP-binding cassette transporters: a proposed two-cylinder engine model.Towards the molecular mechanism of prokaryotic and eukaryotic multidrug transporters.Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1ABC transporters and drug resistance in parasitic protozoa.The multidrug transporter LmrP protein mediates selective calcium efflux.Similarities between ATP-dependent and ion-coupled multidrug transporters.New light on multidrug binding by an ATP-binding-cassette transporter.Molecular disruption of the power stroke in the ATP-binding cassette transport protein MsbA.ABCG transporters: structure, substrate specificities and physiological roles : a brief overview.Substrate binding stabilizes a pre-translocation intermediate in the ATP-binding cassette transport protein MsbAMolecular basis of multidrug transport by ABC transporters.The choreography of multidrug export.
P50
Q26797459-CA959573-347B-40F6-A710-717F709BBB8FQ27684301-11482F85-33CB-4B6B-AD5D-9C5F0CF61987Q28139376-6A1DC68F-0815-4BEF-83B7-003D8CC6C04CQ28484084-B45C69B4-BCC0-4F43-9995-E332D5A273EFQ28550708-F541BEB5-1380-4159-912E-897D973C4DD8Q28728211-796A867F-F2FC-48FC-9BE9-74CF8998A182Q28776849-5A04A105-EDA0-49A8-9BE3-2C70C20569F5Q28817947-02650D0E-0FB6-49AD-A772-28764715D1F8Q28830840-9B07C8B9-1CDB-47D2-B86A-5FCBE327C5EEQ30046461-DBA341C2-BA32-4667-AF6B-630CE98C0A2FQ33179049-1829CB62-3AD7-4BD4-A87E-1067BC044E2EQ33179255-3EC78BF9-7D22-487F-8780-06189485FA3AQ33180064-03BA6597-B679-4651-8B57-0AEDC6958F49Q33182462-F368B79D-1E9A-4A17-95B3-8949C1B52C00Q33187645-E210F09E-93BB-4E72-8310-601DE1D43A20Q33223264-F7AD5FB5-15C6-447C-93AB-0682B538D59DQ33358879-CAF80682-D966-473F-9766-8C14AA79DF3EQ33370616-D26519DC-844E-4C33-B62F-EB185B0F12ADQ33481004-3F780FBB-C25D-4BAE-84C8-6A9C44D11886Q33652073-A80617E3-F1D5-421C-9BB7-89E2D07CA826Q33675820-EE2B5E39-E8C7-42B4-8042-DD07942292C7Q33758020-64B4660C-1DCD-4139-8B39-01BE2D74122DQ33767171-D17A1CB2-CA10-45C8-B589-0CD42C4B0FAEQ33784403-02E73EE2-5A4A-4AE9-A6FD-BD4F9DDE0A78Q33790418-451FD0CD-56EB-4CD4-A281-6A6845E7E752Q33876897-C5135C74-FC08-4320-8D5B-8318EA7C66A9Q33897307-E5A5BDD7-E534-4F8E-98F5-6A3615566361Q34165562-B402FF0E-EF0C-4F10-BC98-7EA236B5976CQ34231096-EA867043-5298-420F-867A-D9AA1C471A1AQ34294752-26AB2DED-F0BF-46B5-9CD2-15875FAE0BA0Q35007411-A2C77809-CF4E-4666-A5C0-8DBD7F9C243DQ35295718-F809DD4A-BCA2-4A41-8C0A-EBF74D935064Q36201981-F364981C-19A0-40AF-B6E9-8DD9CD32AFF6Q36295293-A94C13A0-E5AC-4C9D-8017-CB801BE7A364Q36424404-0FE9577E-4166-454F-872A-454146C739AAQ36666092-2F33F2F0-2E98-40D3-8621-E6FB124D58B6Q36996231-4156F6BE-2CE9-4AE9-8665-1D41BFB162F2Q37048357-DCBC481D-D020-4E3B-84B1-1688DE95E035Q37365936-F078B64E-3FD2-4BD6-A0F5-5D7A1D87FF32Q37877762-3B911CF3-494A-4D8F-9B84-C65CC724F9E2
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Hendrik W van Veen
@ast
Hendrik W van Veen
@en
Hendrik W van Veen
@es
Hendrik W van Veen
@nl
type
label
Hendrik W van Veen
@ast
Hendrik W van Veen
@en
Hendrik W van Veen
@es
Hendrik W van Veen
@nl
altLabel
Hendrik van Veen
@en
prefLabel
Hendrik W van Veen
@ast
Hendrik W van Veen
@en
Hendrik W van Veen
@es
Hendrik W van Veen
@nl
P106
P166
P21
P31
P496
0000-0002-9658-8077